Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases?
Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrol...
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ftdoajarticles:oai:doaj.org/article:cf4b12b9443d46a2a4c0cb885267d58f 2023-05-15T13:33:32+02:00 Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? Isabel Bordes José Recatalá Katarzyna Świderek Vicent Moliner 2015-09-01T00:00:00Z https://doi.org/10.3390/molecules201017789 https://doaj.org/article/cf4b12b9443d46a2a4c0cb885267d58f EN eng MDPI AG http://www.mdpi.com/1420-3049/20/10/17789 https://doaj.org/toc/1420-3049 1420-3049 doi:10.3390/molecules201017789 https://doaj.org/article/cf4b12b9443d46a2a4c0cb885267d58f Molecules, Vol 20, Iss 10, Pp 17789-17806 (2015) Candida antarctica lipase B CALB epoxide hydrolase sEH reaction mechanism trans-diphenylpropene oxide enzyme promiscuity catalysis quantum cluster models Organic chemistry QD241-441 article 2015 ftdoajarticles https://doi.org/10.3390/molecules201017789 2022-12-30T21:27:16Z Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrolase (sEH) formed by a nucleophile-histidine-acid catalytic triad and an oxyanion hole typical for molecular structures derived from processes of α/β hydrolases. In this work we are exploring these similarities and proposing a Ser105Asp variant of CALB as a new catalyst for epoxide hydrolysis. In particular, the hydrolysis of the trans-diphenylpropene oxide (t-DPPO) is studied by means of quantum cluster models mimicking the active site of both enzymes. Our results, based on semi-empirical and DFT calculations, suggest that mutant Ser105Asp CALB is a good protein scaffold to be used for the bio-synthesis of chiral compounds. Article in Journal/Newspaper Antarc* Antarctica Directory of Open Access Journals: DOAJ Articles Molecules 20 10 17789 17806 |
institution |
Open Polar |
collection |
Directory of Open Access Journals: DOAJ Articles |
op_collection_id |
ftdoajarticles |
language |
English |
topic |
Candida antarctica lipase B CALB epoxide hydrolase sEH reaction mechanism trans-diphenylpropene oxide enzyme promiscuity catalysis quantum cluster models Organic chemistry QD241-441 |
spellingShingle |
Candida antarctica lipase B CALB epoxide hydrolase sEH reaction mechanism trans-diphenylpropene oxide enzyme promiscuity catalysis quantum cluster models Organic chemistry QD241-441 Isabel Bordes José Recatalá Katarzyna Świderek Vicent Moliner Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
topic_facet |
Candida antarctica lipase B CALB epoxide hydrolase sEH reaction mechanism trans-diphenylpropene oxide enzyme promiscuity catalysis quantum cluster models Organic chemistry QD241-441 |
description |
Candida Antarctica lipase B (CALB) is a well-known enzyme, especially because of its promiscuous activity. Due to its properties, CALB was widely used as a benchmark for designing new catalysts for important organic reactions. The active site of CALB is very similar to that of soluble epoxide hydrolase (sEH) formed by a nucleophile-histidine-acid catalytic triad and an oxyanion hole typical for molecular structures derived from processes of α/β hydrolases. In this work we are exploring these similarities and proposing a Ser105Asp variant of CALB as a new catalyst for epoxide hydrolysis. In particular, the hydrolysis of the trans-diphenylpropene oxide (t-DPPO) is studied by means of quantum cluster models mimicking the active site of both enzymes. Our results, based on semi-empirical and DFT calculations, suggest that mutant Ser105Asp CALB is a good protein scaffold to be used for the bio-synthesis of chiral compounds. |
format |
Article in Journal/Newspaper |
author |
Isabel Bordes José Recatalá Katarzyna Świderek Vicent Moliner |
author_facet |
Isabel Bordes José Recatalá Katarzyna Świderek Vicent Moliner |
author_sort |
Isabel Bordes |
title |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_short |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_full |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_fullStr |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_full_unstemmed |
Is Promiscuous CALB a Good Scaffold for Designing New Epoxidases? |
title_sort |
is promiscuous calb a good scaffold for designing new epoxidases? |
publisher |
MDPI AG |
publishDate |
2015 |
url |
https://doi.org/10.3390/molecules201017789 https://doaj.org/article/cf4b12b9443d46a2a4c0cb885267d58f |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Molecules, Vol 20, Iss 10, Pp 17789-17806 (2015) |
op_relation |
http://www.mdpi.com/1420-3049/20/10/17789 https://doaj.org/toc/1420-3049 1420-3049 doi:10.3390/molecules201017789 https://doaj.org/article/cf4b12b9443d46a2a4c0cb885267d58f |
op_doi |
https://doi.org/10.3390/molecules201017789 |
container_title |
Molecules |
container_volume |
20 |
container_issue |
10 |
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17789 |
op_container_end_page |
17806 |
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1766043143091781632 |